A. Varga, Z. Bata, Pál Csuka, Diana Monica Bordea, B. Vértessy, A. Marcovici, F. Irimie, L. Poppe, L. Bencze
{"title":"A novel phenylalanine ammonia-lyase from Kangiella koreensis","authors":"A. Varga, Z. Bata, Pál Csuka, Diana Monica Bordea, B. Vértessy, A. Marcovici, F. Irimie, L. Poppe, L. Bencze","doi":"10.24193/SUBBCHEM.2017.3.25","DOIUrl":null,"url":null,"abstract":"This study describes the cloning of the gene encoding a novel phenylalanine ammonia-lyase from Kangiella koreensis (KkPAL) into pET19b expression vector. Optimization of protein expression and purification conditions yielded 15 mg pure soluble protein from one liter of E. coli culture. Enzymatic activity measurements of the ammonia elimination reaction from different natural aromatic amino acids proved the protein to be a phenylalanine ammonia-lyase. The isolated protein showed remarkably high, 81.7 °C melting temperature, making it especially suitable for biocatalytic applications.","PeriodicalId":22005,"journal":{"name":"Studia Universitatis Babes-bolyai Chemia","volume":"1 1","pages":"293-308"},"PeriodicalIF":0.5000,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"7","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Studia Universitatis Babes-bolyai Chemia","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.24193/SUBBCHEM.2017.3.25","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 7
Abstract
This study describes the cloning of the gene encoding a novel phenylalanine ammonia-lyase from Kangiella koreensis (KkPAL) into pET19b expression vector. Optimization of protein expression and purification conditions yielded 15 mg pure soluble protein from one liter of E. coli culture. Enzymatic activity measurements of the ammonia elimination reaction from different natural aromatic amino acids proved the protein to be a phenylalanine ammonia-lyase. The isolated protein showed remarkably high, 81.7 °C melting temperature, making it especially suitable for biocatalytic applications.
期刊介绍：
Studia Universitatis Babes-Bolyai, Seria Chemia publishes fundamental studies in all areas of chemistry and chemical engineering.
Coverage includes experimental and theoretical reports on quantitative studies of structure and thermodynamics, kinetics, mechanisms of reactions, inorganic, organic, organometallic chemistry, biochemistry, computational chemistry, solid-state phenomena, surface chemistry, chemical technology and environmental chemistry.
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
